title: Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of an ASCH domain-containing protein from Zymomonas mobilis ZM4.
abstract: The human activating signal cointegrator 1 (ASC-1) homology (ASCH) domain is frequently observed in many organisms, although its function has not yet been clearly defined. In Zymomonas mobilis ZM4, the ZMO0922 gene encodes a polypeptide that includes an ASCH domain (zmASCH). To provide a better structural background for the probable role of ASCH domain-containing proteins, the ZMO0922 gene was cloned and expressed. The purified protein was crystallized from 30%(w/v) polyethylene glycol 400, 0.1 M cacodylic acid pH 6.5 and 0.2 M lithium sulfate. Diffraction data were collected to 2.1 Å resolution using synchrotron radiation. The crystal belonged to the primitive trigonal space group P3(1)21 or P3(2)21, with unit-cell parameters a=b=51.67, c=207.30 Å, α=β=90, γ=120°. Assuming the presence of one molecule in the asymmetric unit gave a Matthews coefficient of 4.69 Å(3) Da(-1), corresponding to a solvent content of 73.7%.
authors.affiliation: Department of Chemistry, Chonnam National University, Gwangju 500-757, Republic of Korea.
authors.forename: Suk-Youl
authors.initials: SY
authors.lastname: Park
authors.forename: Jeong-Hoh
authors.initials: JH
authors.lastname: Park
authors.forename: Jeong-Sun
authors.initials: JS
authors.lastname: Kim
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D017355:Zymomonas / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; D011994:Recombinant Proteins